Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase

  • Bioorg Med Chem. 2001 Feb;9(2):503-10. doi: 10.1016/s0968-0896(00)00257-1.
S Bounaga  1 ,  M Galleni ,  A P Laws ,  M I Page
Affiliations
  • 1. Department of Chemical and Biological Sciences, University of Huddersfield, Queensgate, UK.
PMID: 11249142 DOI: 10.1016/s0968-0896(00)00257-1
Abstract

Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-beta-lactamase. The pH dependence of pKi indicates that the thiol anion displaces hydroxide ion from the active site zinc(II). D,D-Peptides bind to the enzyme better than Other diastereoisomers, which is compatible with the predicted stereochemistry of the active site.

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